Increasing cytochrome P450 enzyme diversity by identification of two distinct cyclodipeptide dimerases
Genome mining revealed the presence of two cdps-p 450 operons in Saccharopolyspora antimicrobica . Heterologous expression, biochemical characterisation and structure elucidation proved that the two P450 enzymes catalyse distinct regio- and stereospecific dimerizations of cyclo -( l -Trp- l -Trp), w...
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| Published in | Chemical communications (Cambridge, England) Vol. 56; no. 75; pp. 1142 - 1145 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Royal Society of Chemistry
22.09.2020
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| Subjects | |
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| Abstract | Genome mining revealed the presence of two
cdps-p
450 operons in
Saccharopolyspora antimicrobica
. Heterologous expression, biochemical characterisation and structure elucidation proved that the two P450 enzymes catalyse distinct regio- and stereospecific dimerizations of
cyclo
-(
l
-Trp-
l
-Trp), which significantly expands the repertoire of diketopiperazine-tailoring enzymes. TtpB1 connects the monomers
via
C3-C3′, both from the opposite side of H-11/H-11′, while TtpB2 is characterised as the first P450 to mainly catalyse the unusual linkage between N1′ and C3 from the H-11 side.
Two P450 enzymes were characterised to catalyse distinct regio- and stereospecific dimerizations of
cyclo
-(
l
-Trp-
l
-Trp), differing from those previously reported in actinobacteria. |
|---|---|
| AbstractList | Genome mining revealed the presence of two cdps-p450 operons in Saccharopolyspora antimicrobica. Heterologous expression, biochemical characterisation and structure elucidation proved that the two P450 enzymes catalyse distinct regio- and stereospecific dimerizations of cyclo-(l-Trp-l-Trp), which significantly expands the repertoire of diketopiperazine-tailoring enzymes. TtpB1 connects the monomers via C3-C3', both from the opposite side of H-11/H-11', while TtpB2 is characterised as the first P450 to mainly catalyse the unusual linkage between N1' and C3 from the H-11 side.Genome mining revealed the presence of two cdps-p450 operons in Saccharopolyspora antimicrobica. Heterologous expression, biochemical characterisation and structure elucidation proved that the two P450 enzymes catalyse distinct regio- and stereospecific dimerizations of cyclo-(l-Trp-l-Trp), which significantly expands the repertoire of diketopiperazine-tailoring enzymes. TtpB1 connects the monomers via C3-C3', both from the opposite side of H-11/H-11', while TtpB2 is characterised as the first P450 to mainly catalyse the unusual linkage between N1' and C3 from the H-11 side. Genome mining revealed the presence of two cdps-p450 operons in Saccharopolyspora antimicrobica. Heterologous expression, biochemical characterisation and structure elucidation proved that the two P450 enzymes catalyse distinct regio- and stereospecific dimerizations of cyclo-(l-Trp-l-Trp), which significantly expands the repertoire of diketopiperazine-tailoring enzymes. TtpB1 connects the monomers via C3–C3′, both from the opposite side of H-11/H-11′, while TtpB2 is characterised as the first P450 to mainly catalyse the unusual linkage between N1′ and C3 from the H-11 side. Genome mining revealed the presence of two cdps-p 450 operons in Saccharopolyspora antimicrobica . Heterologous expression, biochemical characterisation and structure elucidation proved that the two P450 enzymes catalyse distinct regio- and stereospecific dimerizations of cyclo -( l -Trp- l -Trp), which significantly expands the repertoire of diketopiperazine-tailoring enzymes. TtpB1 connects the monomers via C3–C3′, both from the opposite side of H-11/H-11′, while TtpB2 is characterised as the first P450 to mainly catalyse the unusual linkage between N1′ and C3 from the H-11 side. Genome mining revealed the presence of two cdps-p 450 operons in Saccharopolyspora antimicrobica . Heterologous expression, biochemical characterisation and structure elucidation proved that the two P450 enzymes catalyse distinct regio- and stereospecific dimerizations of cyclo -( l -Trp- l -Trp), which significantly expands the repertoire of diketopiperazine-tailoring enzymes. TtpB1 connects the monomers via C3-C3′, both from the opposite side of H-11/H-11′, while TtpB2 is characterised as the first P450 to mainly catalyse the unusual linkage between N1′ and C3 from the H-11 side. Two P450 enzymes were characterised to catalyse distinct regio- and stereospecific dimerizations of cyclo -( l -Trp- l -Trp), differing from those previously reported in actinobacteria. |
| Author | Liu, Jing Li, Shu-Ming Xie, Xiulan |
| AuthorAffiliation | Philipps-Universität Marburg Fachbereich Chemie Institut für Pharmazeutische Biologie und Biotechnologie Fachbereich Pharmazie |
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| Snippet | Genome mining revealed the presence of two
cdps-p
450 operons in
Saccharopolyspora antimicrobica
. Heterologous expression, biochemical characterisation and... Genome mining revealed the presence of two cdps-p450 operons in Saccharopolyspora antimicrobica. Heterologous expression, biochemical characterisation and... |
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| SubjectTerms | cytochrome P-450 Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - genetics Cytochrome P-450 Enzyme System - metabolism Cytochromes P450 Dimerization Enzymes heterologous gene expression Molecular Conformation operon Peptides, Cyclic - chemistry Peptides, Cyclic - genetics Peptides, Cyclic - metabolism Saccharopolyspora Saccharopolyspora - enzymology stereospecificity |
| Title | Increasing cytochrome P450 enzyme diversity by identification of two distinct cyclodipeptide dimerases |
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